Analytical Data
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Gene name
FBLN4
- Application
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Alternative Names
FBLN4；FBLN4；EGF-containing fibulin-like extracellular matrix Protein 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95967
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Expression Region
26-443aa
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AA Sequence
SPQDS EEPDSYTECT DGYEWDPDSQ HCRDVNECLT IPEACKGEMK CINHYGGYLC LPRSAAVIND LHGEGPPPPV PPAQHPNPCP PGYEPDDQDS CVDVDECAQA LHDCRPSQDC HNLPGSYQCT CPDGYRKIGP ECVDIDECRY RYCQHRCVNL PGSFRCQCEP GFQLGPNNRS CVDVNECDMG APCEQRCFNS YGTFLCRCHQ GYELHRDGFS CSDIDECSYS SYLCQYRCIN EPGRFSCHCP QGYQLLATRL CQDIDECESG AHQCSEAQTC VNFHGGYRCV DTNRCVEPYI QVSENRCLCP ASNPLCREQP SSIVHRYMTI TSERSVPADV FQIQATSVYP GAYNAFQIRA GNSQGDFYIR QINNVSAMLV LARPVTGPRE YVLDLEMVTM NSLMSYRASS VLRLTVFVGA YTF
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
The study of FBLN4 (fibulin-4) recombinant protein has garnered significant interest due to its crucial role in extracellular matrix (ECM) organization and angiogenesis. FBLN4 is a member of the fibulin family, which consists of glycoproteins that contribute to the structural integrity of tissues by interacting with various ECM components and cell surface receptors. Research has shown that FBLN4 is particularly important in the development and maintenance of vascular tissues, influencing processes such as endothelial cell behavior and tissue remodeling. Abnormalities or mutations in the FBLN4 gene have been linked to cardiovascular diseases and congenital vascular malformations, highlighting its clinical significance. The recombinant production of FBLN4 provides a valuable tool for investigating its functional properties and potential therapeutic applications. By producing this protein in a controlled environment, researchers can study its interactions with other ECM proteins and its effects on cell signaling pathways. This knowledge might pave the way for novel strategies in treating diseases related to ECM dysregulation. Furthermore, understanding the molecular mechanisms by which FBLN4 contributes to vascular development could lead to the identification of biomarkers for diseases and inform the design of targeted therapies. Given the increasing prevalence of cardiovascular disorders globally, the exploration of FBLN4’s role in cardiovascular health and disease represents a promising avenue of research that may ultimately lead to innovative treatment approaches.
